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Volumn 24, Issue 3, 1997, Pages 579-591

The cioAB genes from Pseudomonas aeruginosa code for a novel cyanide- insensitive terminal oxidase related to the cytochrome bd quinol oxidases

Author keywords

[No Author keywords available]

Indexed keywords

CYANIDE; CYTOCHROME B; CYTOCHROME C OXIDASE; CYTOCHROME D; HEME;

EID: 0030915436     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1997.3561728.x     Document Type: Article
Times cited : (112)

References (69)
  • 1
    • 0019888537 scopus 로고
    • Evidence for two functional gal promoters in intact Escherichia coli cells
    • Aiba, H., Adhya, S., and De Crombrugghe, B. (1981) Evidence for two functional gal promoters in intact Escherichia coli cells. J Biol Chem 256: 1905-1910.
    • (1981) J Biol Chem , vol.256 , pp. 1905-1910
    • Aiba, H.1    Adhya, S.2    De Crombrugghe, B.3
  • 2
    • 0021284981 scopus 로고
    • On the absence of correlation between cyanide-resistant respiration and cytochrome d content in bacteria
    • Akimenko, V.K., and Trutko, S.M. (1984) On the absence of correlation between cyanide-resistant respiration and cytochrome d content in bacteria. Arch Microbiol 138: 58-63.
    • (1984) Arch Microbiol , vol.138 , pp. 58-63
    • Akimenko, V.K.1    Trutko, S.M.2
  • 3
    • 0029146375 scopus 로고
    • Expression of the nir and nor genes for denitrification of Pseudomonas aeruginosa requires a novel CRP/FNR-related transcriptional regulator, Dnr, in addition to Anr
    • Arai, H., Igarashi, Y., and Kodama, T. (1995) Expression of the nir and nor genes for denitrification of Pseudomonas aeruginosa requires a novel CRP/FNR-related transcriptional regulator, Dnr, in addition to Anr. FEBS Lett 371: 73-76.
    • (1995) FEBS Lett , vol.371 , pp. 73-76
    • Arai, H.1    Igarashi, Y.2    Kodama, T.3
  • 4
    • 0013852796 scopus 로고
    • Etude de la cytochrome-oxidase de Pseudomonas aeruginosa
    • Azoulay, E., and Couchoud-Beaumont, P. (1965) Etude de la cytochrome-oxidase de Pseudomonas aeruginosa. Biochem Biophys Acta 110: 301-311.
    • (1965) Biochem Biophys Acta , vol.110 , pp. 301-311
    • Azoulay, E.1    Couchoud-Beaumont, P.2
  • 5
    • 0016717640 scopus 로고
    • The effect of temperature on the cytochrome pattern and respiration of Pseudomonas aeruginosa
    • Calcott, P.H., Bhatti, A.R., and Ingram, J.M. (1975) The effect of temperature on the cytochrome pattern and respiration of Pseudomonas aeruginosa. FEBS Lett 56: 318-321.
    • (1975) FEBS Lett , vol.56 , pp. 318-321
    • Calcott, P.H.1    Bhatti, A.R.2    Ingram, J.M.3
  • 6
    • 0028137093 scopus 로고
    • The cytochrome oxidase superfamily of redox driven proton pumps
    • Calhoun, M.W., Thomas, J.W., and Gennis, R.B. (1994) The cytochrome oxidase superfamily of redox driven proton pumps. Trends Biochem Sci 19: 325-330.
    • (1994) Trends Biochem Sci , vol.19 , pp. 325-330
    • Calhoun, M.W.1    Thomas, J.W.2    Gennis, R.B.3
  • 7
    • 0021012711 scopus 로고
    • Hydrogen cyanide production by Pseudomonas aeruginosa at reduced oxygen levels
    • Castric, P.A. (1983) Hydrogen cyanide production by Pseudomonas aeruginosa at reduced oxygen levels. Can J Microbiol 29: 1344-1349.
    • (1983) Can J Microbiol , vol.29 , pp. 1344-1349
    • Castric, P.A.1
  • 8
    • 0025129999 scopus 로고
    • Cytochrome o (cyo ABCDE) and d (cydAB) oxidase gene expression in Escherchia coli is regulated by oxygen, pH and the fnr gene product
    • Cotter, P.A., Chepuri, V., Gennis, R.B., and Gunsalus, R.P. (1990) Cytochrome o (cyo ABCDE) and d (cydAB) oxidase gene expression in Escherchia coli is regulated by oxygen, pH and the fnr gene product. J Bacteriol 172: 6333-6338.
    • (1990) J Bacteriol , vol.172 , pp. 6333-6338
    • Cotter, P.A.1    Chepuri, V.2    Gennis, R.B.3    Gunsalus, R.P.4
  • 9
    • 0028854401 scopus 로고
    • Isolation and characterisation of mutants defective in the cyanide-insensitive respiratory pathway of Pseudomonas aeruginosa
    • Cunningham, L., and Williams, H.D. (1995) Isolation and characterisation of mutants defective in the cyanide-insensitive respiratory pathway of Pseudomonas aeruginosa. J Bacteriol 177: 432-438.
    • (1995) J Bacteriol , vol.177 , pp. 432-438
    • Cunningham, L.1    Williams, H.D.2
  • 10
    • 0026006133 scopus 로고
    • A new oxygen-regulated operon in Escherichia coli comprises the genes for a putative third cytochrome oxidase and for pH 2.5 acid phosphatase (appA)
    • Dassa, J., Fsihi, H., Marck, C., Dion, M., Kieffer-Bontemps, M., and Boquet, P.L. (1991) A new oxygen-regulated operon in Escherichia coli comprises the genes for a putative third cytochrome oxidase and for pH 2.5 acid phosphatase (appA). Mol Gen Genet 229: 341-352.
    • (1991) Mol Gen Genet , vol.229 , pp. 341-352
    • Dassa, J.1    Fsihi, H.2    Marck, C.3    Dion, M.4    Kieffer-Bontemps, M.5    Boquet, P.L.6
  • 11
    • 0028263624 scopus 로고
    • Determination of the oxygen affinities of terminal oxidases in Azotobacter vinelandii using the deoxygenation of oxyleghemoglobin and oxymyoglobin - Cytochrome bd is a low affinity oxidase
    • D'Mello, R., Hill, S., and Poole, R.K. (1994) Determination of the oxygen affinities of terminal oxidases in Azotobacter vinelandii using the deoxygenation of oxyleghemoglobin and oxymyoglobin - cytochrome bd is a low affinity oxidase. Microbiol 140: 1395-1402.
    • (1994) Microbiol , vol.140 , pp. 1395-1402
    • D'Mello, R.1    Hill, S.2    Poole, R.K.3
  • 12
    • 0029981912 scopus 로고    scopus 로고
    • The cytochrome bd quinol oxidase in Escherichia coli has an extremely high apparent affinity for oxygen and two oxygen-binding haems: Implications for regulation of activity in vivo by substrate (oxygen) inhibition
    • D'Mello, R., Hill, S., and Poole, R.K. (1996) The cytochrome bd quinol oxidase in Escherichia coli has an extremely high apparent affinity for oxygen and two oxygen-binding haems: implications for regulation of activity in vivo by substrate (oxygen) inhibition. Microbiol 142: 755-763.
    • (1996) Microbiol , vol.142 , pp. 755-763
    • D'Mello, R.1    Hill, S.2    Poole, R.K.3
  • 13
    • 0025259440 scopus 로고
    • Epitopes of monoclonal antibodies which inhibit ubiquinol oxidase activity of Escherichia coli cytochrome d complex localize a functional domain
    • Dueweke, T.J., and Gennis, R.B. (1990) Epitopes of monoclonal antibodies which inhibit ubiquinol oxidase activity of Escherichia coli cytochrome d complex localize a functional domain. J Biol Chem 265: 4273-4277.
    • (1990) J Biol Chem , vol.265 , pp. 4273-4277
    • Dueweke, T.J.1    Gennis, R.B.2
  • 14
    • 0025881879 scopus 로고
    • Proteolysis of the cytochrome d complex with trypsin and chymotrypsin localises a quinol oxidase domain
    • Dueweke, T.J., and Gennis, R.B. (1991) Proteolysis of the cytochrome d complex with trypsin and chymotrypsin localises a quinol oxidase domain. Biochem 30: 3401-3406.
    • (1991) Biochem , vol.30 , pp. 3401-3406
    • Dueweke, T.J.1    Gennis, R.B.2
  • 15
    • 0024411033 scopus 로고
    • Location of haem axial ligands in the cytochrome d terminal oxidase complex of Escherichia coli determined by site directed mutagenesis
    • Fang, H., Lin, R.-J., and Gennis, R.B. (1989) Location of haem axial ligands in the cytochrome d terminal oxidase complex of Escherichia coli determined by site directed mutagenesis. J Biol Chem 264: 8026-8032.
    • (1989) J Biol Chem , vol.264 , pp. 8026-8032
    • Fang, H.1    Lin, R.-J.2    Gennis, R.B.3
  • 16
    • 0025453157 scopus 로고
    • High efficiency electroporation of Pseudomonas aeruginosa using frozen cell suspensions
    • Farinha, M.A., and Kropinski, A.M. (1990) High efficiency electroporation of Pseudomonas aeruginosa using frozen cell suspensions. FEMS Microbiol Lett 70: 221-226.
    • (1990) FEMS Microbiol Lett , vol.70 , pp. 221-226
    • Farinha, M.A.1    Kropinski, A.M.2
  • 17
    • 0026663123 scopus 로고
    • 3, purified from aerobically grown Pseudomonas aeruginosa: It shows a clear difference between resting state and pulsed state
    • 3, purified from aerobically grown Pseudomonas aeruginosa: it shows a clear difference between resting state and pulsed state. J Biochem 223: 290-298.
    • (1992) J Biochem , vol.223 , pp. 290-298
    • Fujiwara, T.1    Fukumari, Y.2    Yamanaka, T.3
  • 19
    • 0023750080 scopus 로고
    • β-galactosidase gene fusions as probes for the cytoplasmic regions of subunit I and II of the membrane-bound cytochrome d terminal oxidase from Escherichia coli
    • Georgiou, C.D., Dueweke, T.J., and Gennis, R.B. (1988) β-galactosidase gene fusions as probes for the cytoplasmic regions of subunit I and II of the membrane-bound cytochrome d terminal oxidase from Escherichia coli. J Biol Chem 263: 13130-13137.
    • (1988) J Biol Chem , vol.263 , pp. 13130-13137
    • Georgiou, C.D.1    Dueweke, T.J.2    Gennis, R.B.3
  • 20
    • 0014045168 scopus 로고
    • Cyanide production by Pseudomonas aeruginosa
    • Goldfarb, W.B., and Margraf, H. (1967) Cyanide production by Pseudomonas aeruginosa. Ann Surg 165: 104-110.
    • (1967) Ann Surg , vol.165 , pp. 104-110
    • Goldfarb, W.B.1    Margraf, H.2
  • 21
    • 0028276785 scopus 로고
    • Regulation of transcription at the ndh promoter of Escherichia coli by Fnr and novel factors
    • Green, J., and Guest, J.R. (1994) Regulation of transcription at the ndh promoter of Escherichia coli by Fnr and novel factors. Mol Microbiol 12: 433-444.
    • (1994) Mol Microbiol , vol.12 , pp. 433-444
    • Green, J.1    Guest, J.R.2
  • 22
    • 0023802457 scopus 로고
    • The nucleotide sequence of the cyd locus encoding the two subunits of the cytochrome d terminal oxidase complex of Escherichia coli
    • Green, N.G., Fang, H., Lin, R.-J., Newton, G., Mather, M., Georgiou, C.D., and Gennis, R.B. (1988) The nucleotide sequence of the cyd locus encoding the two subunits of the cytochrome d terminal oxidase complex of Escherichia coli. J Biol Chem 263: 13138-13143.
    • (1988) J Biol Chem , vol.263 , pp. 13138-13143
    • Green, N.G.1    Fang, H.2    Lin, R.-J.3    Newton, G.4    Mather, M.5    Georgiou, C.D.6    Gennis, R.B.7
  • 24
    • 0023650036 scopus 로고
    • Electron flow and haem-haem interaction between cytochromes b-558, b-595 and d in a terminal oxidase of Escherichia coli
    • Hata-Tanaka, A., Matsuura, K., Itoh, S., and Anraku, Y. (1987) Electron flow and haem-haem interaction between cytochromes b-558, b-595 and d in a terminal oxidase of Escherichia coli. Biochim Biophys Acta 893: 289-295.
    • (1987) Biochim Biophys Acta , vol.893 , pp. 289-295
    • Hata-Tanaka, A.1    Matsuura, K.2    Itoh, S.3    Anraku, Y.4
  • 25
    • 0027299607 scopus 로고
    • Spectroscopic evidence for a haem-haem binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli
    • Hill, J.J., Alben, J.O., and Gennis, R.B. (1993) Spectroscopic evidence for a haem-haem binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli. Proc Natl Acad Sci USA 90: 5863-5867.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5863-5867
    • Hill, J.J.1    Alben, J.O.2    Gennis, R.B.3
  • 26
    • 84984233402 scopus 로고
    • Resonance Raman study on axial ligands of heme irons in cytochrome tod-type terminal oxidase from Escherichia coli
    • Hirota, S., Mogi, T., Anraku, Y., Gennis, R.B., and Kitagawa, T. (1995) Resonance Raman study on axial ligands of heme irons in cytochrome tod-type terminal oxidase from Escherichia coli. Biospectroscopy 1: 305-311.
    • (1995) Biospectroscopy , vol.1 , pp. 305-311
    • Hirota, S.1    Mogi, T.2    Anraku, Y.3    Gennis, R.B.4    Kitagawa, T.5
  • 27
    • 0025144171 scopus 로고
    • Requirement for terminal cytochromes in generation of the aerobic signal for the arc regulatory system in Escherichia coli: Study using deletions and lac fusions of cyo and cyd
    • Iuchi, S., Chepuri, V., Fu, H.-A., Gennis, R.B., and Lin, E.C.C. (1990) Requirement for terminal cytochromes in generation of the aerobic signal for the arc regulatory system in Escherichia coli: study using deletions and lac fusions of cyo and cyd. J Bacteriol 172: 6070-6025.
    • (1990) J Bacteriol , vol.172 , pp. 6070-16025
    • Iuchi, S.1    Chepuri, V.2    Fu, H.-A.3    Gennis, R.B.4    Lin, E.C.C.5
  • 28
  • 29
    • 0001689585 scopus 로고
    • Analysis of cytochromes
    • Jones, C.W., and Poole, R.K. (1985) Analysis of cytochromes. Meth Microbiol 18: 285-328.
    • (1985) Meth Microbiol , vol.18 , pp. 285-328
    • Jones, C.W.1    Poole, R.K.2
  • 31
    • 0025030204 scopus 로고
    • Cloning and mutagenesis of genes encoding the cytochrome bd terminal oxidase complex in Azotobacter vinelandii: Mutants deficient in the cytochrome d complex are unable to fix nitrogen in air
    • Kelly, M.J.S., Poole, R.K., Yates, M.G., and Kennedy, C. (1990) Cloning and mutagenesis of genes encoding the cytochrome bd terminal oxidase complex in Azotobacter vinelandii: mutants deficient in the cytochrome d complex are unable to fix nitrogen in air. J Bacteriol 172: 6010-6019.
    • (1990) J Bacteriol , vol.172 , pp. 6010-6019
    • Kelly, M.J.S.1    Poole, R.K.2    Yates, M.G.3    Kennedy, C.4
  • 32
    • 0015517591 scopus 로고
    • A new purification procedure and molecular properties of Pseudomonas cytochrome oxidase
    • Kuronen, T., and Ellfork, N. (1972) A new purification procedure and molecular properties of Pseudomonas cytochrome oxidase. Biochem Biophys Acta 275: 308-318.
    • (1972) Biochem Biophys Acta , vol.275 , pp. 308-318
    • Kuronen, T.1    Ellfork, N.2
  • 33
    • 0020475449 scopus 로고
    • A simple method for displaying the hydrophobic character of a protein
    • Kyte, J., and Doolittle, R.F. (1982) A simple method for displaying the hydrophobic character of a protein. J Mol Biol 157: 105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 34
    • 0023645288 scopus 로고
    • Cytochrome b-558 monitors the steady-state redox state of the ubiquinone pool in the aerobic respiratory chain of Escherichia coli
    • Lorence, R.M., Carter, K., Green, G.N., and Gennis, R.B. (1987) Cytochrome b-558 monitors the steady-state redox state of the ubiquinone pool in the aerobic respiratory chain of Escherichia coli. J Biol Chem 262: 10532-10536.
    • (1987) J Biol Chem , vol.262 , pp. 10532-10536
    • Lorence, R.M.1    Carter, K.2    Green, G.N.3    Gennis, R.B.4
  • 35
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell, M.A.K., Haas, S.M., Bieker, L.L., and Tolbert, N.F. (1978) A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal Biochem 87: 206-210.
    • (1978) Anal Biochem , vol.87 , pp. 206-210
    • Markwell, M.A.K.1    Haas, S.M.2    Bieker, L.L.3    Tolbert, N.F.4
  • 36
    • 0018862783 scopus 로고
    • Membrane bound respiratory chain of Pseudomonas aeruginosa grown aerobically
    • Matsushita, K., Yamada, M., Shinagawa, E., Adachi, O., and Ameyama, M. (1980) Membrane bound respiratory chain of Pseudomonas aeruginosa grown aerobically. J Bacteriol 141: 389-392.
    • (1980) J Bacteriol , vol.141 , pp. 389-392
    • Matsushita, K.1    Yamada, M.2    Shinagawa, E.3    Adachi, O.4    Ameyama, M.5
  • 37
    • 0020028248 scopus 로고
    • o-type cytochrome oxidase in the membrane of aerobically grown Pseudomonas aeruginosa
    • Matsushita, K., Shinagawa, E., Adachi, O., and Ameyama, M. (1982) o-type cytochrome oxidase in the membrane of aerobically grown Pseudomonas aeruginosa. FEBS Lett 139: 255-258.
    • (1982) FEBS Lett , vol.139 , pp. 255-258
    • Matsushita, K.1    Shinagawa, E.2    Adachi, O.3    Ameyama, M.4
  • 38
    • 0020743150 scopus 로고
    • Membrane bound respiratory chain of Pseudomonas aeruginosa grown aerobically. A KCN-insensitive alternative oxidase chain and its energetics
    • Matsushita, K., Yamada, M., Shinagawa, E., Adachi, O., and Ameyama, M. (1983) Membrane bound respiratory chain of Pseudomonas aeruginosa grown aerobically. A KCN-insensitive alternative oxidase chain and its energetics. J Biochem 93: 1137-1144.
    • (1983) J Biochem , vol.93 , pp. 1137-1144
    • Matsushita, K.1    Yamada, M.2    Shinagawa, E.3    Adachi, O.4    Ameyama, M.5
  • 39
    • 0024976978 scopus 로고
    • EPR studies of the cytochrome-d complex of Escherichia coli
    • Meinhardt, S.W., Gennis, R.B., and Ohnishi, T. (1989) EPR studies of the cytochrome-d complex of Escherichia coli. Biochim Biophys Acta 975: 175-184.
    • (1989) Biochim Biophys Acta , vol.975 , pp. 175-184
    • Meinhardt, S.W.1    Gennis, R.B.2    Ohnishi, T.3
  • 40
    • 0021099774 scopus 로고
    • The purification and characterisation of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain
    • Miller, M.J., and Gennis, R.B. (1983) The purification and characterisation of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain. J Biol Chem 258: 9159-9165.
    • (1983) J Biol Chem , vol.258 , pp. 9159-9165
    • Miller, M.J.1    Gennis, R.B.2
  • 41
    • 8244260405 scopus 로고
    • The active form of the cytochrome d terminal oxidase complex of Escherichia coli is a heterodimer containing one copy of each of the two subunits
    • Miller, M.J., Hermodson, M., and Gennis, R.B. (1988) The active form of the cytochrome d terminal oxidase complex of Escherichia coli is a heterodimer containing one copy of each of the two subunits. J Biol Chem 261: 4987-4990.
    • (1988) J Biol Chem , vol.261 , pp. 4987-4990
    • Miller, M.J.1    Hermodson, M.2    Gennis, R.B.3
  • 42
    • 0025945337 scopus 로고
    • Cloning, characterisation, and expression in Escherichia coli of the genes encoding the cytochrome d oxidase complex from Azotobacter vinelandii
    • Moshiri, F., Chawla, A., and Maier, R.J. (1991a) Cloning, characterisation, and expression in Escherichia coli of the genes encoding the cytochrome d oxidase complex from Azotobacter vinelandii. J Bacteriol 173: 6230-6241.
    • (1991) J Bacteriol , vol.173 , pp. 6230-6241
    • Moshiri, F.1    Chawla, A.2    Maier, R.J.3
  • 44
    • 0026000311 scopus 로고
    • Analysis of the topology of the cytochrome d oxidase complex of Escherichia coli by alkaline phosphatase fusions
    • Newton, G., Yun, C.-H., and Gennis, R.B. (1991) Analysis of the topology of the cytochrome d oxidase complex of Escherichia coli by alkaline phosphatase fusions. Mol Microbiol 5: 2511-2518.
    • (1991) Mol Microbiol , vol.5 , pp. 2511-2518
    • Newton, G.1    Yun, C.-H.2    Gennis, R.B.3
  • 45
    • 0026555152 scopus 로고
    • PCR amplification of long DNA fragments
    • Ponce, M.R., and Micol, J.L. (1992) PCR amplification of long DNA fragments. Nucleic Acids Res 20: 623.
    • (1992) Nucleic Acids Res , vol.20 , pp. 623
    • Ponce, M.R.1    Micol, J.L.2
  • 46
    • 0003120348 scopus 로고
    • Bacterial cytochrome oxidases
    • Anthony, C. (ed.). London: Academic Press
    • Poole, R.K. (1988) Bacterial cytochrome oxidases. In Bacterial Energy Transduction. Anthony, C. (ed.). London: Academic Press, pp. 231-291.
    • (1988) Bacterial Energy Transduction , pp. 231-291
    • Poole, R.K.1
  • 47
    • 0020627779 scopus 로고
    • The 650 nm chromophore in Escherichia coli is an oxycompound or oxygenated compound, not the oxidised form of cytochrome oxidase d - An hypothesis
    • Poole, R.K., Kumar, C., Salmon, I., and Chance, B. (1983) The 650 nm chromophore in Escherichia coli is an oxycompound or oxygenated compound, not the oxidised form of cytochrome oxidase d - an hypothesis. J Gen Microbiol 129: 1335-1344.
    • (1983) J Gen Microbiol , vol.129 , pp. 1335-1344
    • Poole, R.K.1    Kumar, C.2    Salmon, I.3    Chance, B.4
  • 48
    • 0016277302 scopus 로고
    • Inhibition by cyanide of the respiratory chain oxidases of Escherichia coli
    • Pudek, A.D., and Bragg, P.D. (1974) Inhibition by cyanide of the respiratory chain oxidases of Escherichia coli. Arch Biochem Biophys 164: 682-693.
    • (1974) Arch Biochem Biophys , vol.164 , pp. 682-693
    • Pudek, A.D.1    Bragg, P.D.2
  • 49
    • 0026438826 scopus 로고
    • The low-spin haem site of cytochrome o from Escherichia coli is promiscuous with respect to haem type
    • Puustinen, A., Moyan, J.E., Verkhousky, M., Thomas, J.W., Gennis, R.B., and Wikstrom, M. (1992) The low-spin haem site of cytochrome o from Escherichia coli is promiscuous with respect to haem type. Biochem 31: 10363-10369.
    • (1992) Biochem , vol.31 , pp. 10363-10369
    • Puustinen, A.1    Moyan, J.E.2    Verkhousky, M.3    Thomas, J.W.4    Gennis, R.B.5    Wikstrom, M.6
  • 50
    • 0030057005 scopus 로고    scopus 로고
    • A mutant of Pseudomonas aeruginosa that lacks c-type cytochromes has a functional cyanide-insensitive oxidase
    • Ray, A., and Williams, H.D. (1996) A mutant of Pseudomonas aeruginosa that lacks c-type cytochromes has a functional cyanide-insensitive oxidase. FEMS Microbiol Lett 135: 123-129.
    • (1996) FEMS Microbiol Lett , vol.135 , pp. 123-129
    • Ray, A.1    Williams, H.D.2
  • 51
    • 0017858515 scopus 로고
    • Oxygen-limited continuous culture and respiratory energy conservation in Escherichia coli
    • Rice, C.W., and Hempfling, W.P. (1978) Oxygen-limited continuous culture and respiratory energy conservation in Escherichia coli. J Bacteriol 134: 115-124.
    • (1978) J Bacteriol , vol.134 , pp. 115-124
    • Rice, C.W.1    Hempfling, W.P.2
  • 52
    • 0024348253 scopus 로고
    • Electron paramagnetic study of the cytochrome bd complex in situ
    • Rothery, R., and Ingledew, W.J. (1989) Electron paramagnetic study of the cytochrome bd complex in situ. Biochem J 262: 437-443.
    • (1989) Biochem J , vol.262 , pp. 437-443
    • Rothery, R.1    Ingledew, W.J.2
  • 55
    • 0025866366 scopus 로고
    • Identification and molecular characterisation of a transcriptional regulator from Pseudomonas aeruginosa PAO1 exhibiting structural and functional similarity to the FNR protein of Escherichia coli
    • Sawers, R.G. (1991) Identification and molecular characterisation of a transcriptional regulator from Pseudomonas aeruginosa PAO1 exhibiting structural and functional similarity to the FNR protein of Escherichia coli. Mol Microbiol 5: 1469-1481.
    • (1991) Mol Microbiol , vol.5 , pp. 1469-1481
    • Sawers, R.G.1
  • 56
    • 0026011339 scopus 로고
    • Escherichia-Pseudomonas shuttle vectors derived from pUC18/19
    • Schweizer, H.P. (1991) Escherichia-Pseudomonas shuttle vectors derived from pUC18/19. Gene 97: 109-112.
    • (1991) Gene , vol.97 , pp. 109-112
    • Schweizer, H.P.1
  • 58
    • 0029867565 scopus 로고    scopus 로고
    • Purification of a cytochrome bd terminal oxidase encoded by the Escherichia coli app locus from a Δcyo Δcyd strain complemented by genes from Bacillus firmus OF4
    • Sturr, M.G., Krulwich, T.A., and Hicks, D.B. (1996) Purification of a cytochrome bd terminal oxidase encoded by the Escherichia coli app locus from a Δcyo Δcyd strain complemented by genes from Bacillus firmus OF4. J Bacteriol 176: 1742-1749.
    • (1996) J Bacteriol , vol.176 , pp. 1742-1749
    • Sturr, M.G.1    Krulwich, T.A.2    Hicks, D.B.3
  • 59
    • 0027969974 scopus 로고
    • The ccoNOQP gene cluster codes for a co-type cytochrome oxidase that functions in aerobic respiration of Rhodobacter capsulatus
    • Thöny-Meyer, L., Beck, C., Preisig, O., and Hennecke, H. (1994) The ccoNOQP gene cluster codes for a co-type cytochrome oxidase that functions in aerobic respiration of Rhodobacter capsulatus. Mol Microbiol 14: 705-716.
    • (1994) Mol Microbiol , vol.14 , pp. 705-716
    • Thöny-Meyer, L.1    Beck, C.2    Preisig, O.3    Hennecke, H.4
  • 60
    • 33845378891 scopus 로고
    • Proposed structure of haem d, a prosthetic group of bacterial terminal oxidases
    • Timkovich, R., Cork, M.S., Gennis, R.B., and Johnson, P.Y. (1985) Proposed structure of haem d, a prosthetic group of bacterial terminal oxidases. J Am Chem Soc 107: 6069-6075.
    • (1985) J Am Chem Soc , vol.107 , pp. 6069-6075
    • Timkovich, R.1    Cork, M.S.2    Gennis, R.B.3    Johnson, P.Y.4
  • 61
    • 0028290824 scopus 로고
    • Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration - The enzymology of coupling electron-transfer reactions to transmembrane proton translocation
    • Trumpower, B.L., and Gennis, R.B. (1994) Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration - the enzymology of coupling electron-transfer reactions to transmembrane proton translocation. Ann Rev Biochem 63: 675-716.
    • (1994) Ann Rev Biochem , vol.63 , pp. 675-716
    • Trumpower, B.L.1    Gennis, R.B.2
  • 62
    • 0027482992 scopus 로고
    • Cytochrome d axial ligand of the bd-type quinol oxidase from Escherichia coli
    • Tsubaki, M., Uno, T., Hori, H., Mogi, T., Nishimura, Y., and Anraku, Y. (1993) Cytochrome d axial ligand of the bd-type quinol oxidase from Escherichia coli. FEBS Lett 335: 13-17.
    • (1993) FEBS Lett , vol.335 , pp. 13-17
    • Tsubaki, M.1    Uno, T.2    Hori, H.3    Mogi, T.4    Nishimura, Y.5    Anraku, Y.6
  • 63
    • 0025923703 scopus 로고
    • 1 nitrite reductase from Pseudomonas stutzeri JM300 and reconstitution with native and synthetic haem d
    • 1 nitrite reductase from Pseudomonas stutzeri JM300 and reconstitution with native and synthetic haem d. J Biol Chem 266: 7496-7502.
    • (1991) J Biol Chem , vol.266 , pp. 7496-7502
    • Weeg-Aerssens, E.1    Wu, W.2    Ye, R.W.3    Tiedje, J.M.4    Chang, C.K.5
  • 64
    • 0024284614 scopus 로고
    • Codon usage in Pseudomonas aeruginosa
    • West, S.E.H., and Iglewski, B.H. (1988) Codon usage in Pseudomonas aeruginosa. Nucleic Acids Res 16: 9323-9335.
    • (1988) Nucleic Acids Res , vol.16 , pp. 9323-9335
    • West, S.E.H.1    Iglewski, B.H.2
  • 65
    • 0039985564 scopus 로고
    • 1-like haemoprotein in electron-transfer to cytochrome oxidase d
    • 1-like haemoprotein in electron-transfer to cytochrome oxidase d. J Gen Microbiol 133: 2461-2472.
    • (1987) J Gen Microbiol , vol.133 , pp. 2461-2472
    • Williams, H.D.1    Poole, R.K.2
  • 66
    • 0022608046 scopus 로고
    • Isolation and chracterisation of TMPD-oxidase mutants of Pseudomonas aeruginosa
    • Yang, T. (1986) Isolation and chracterisation of TMPD-oxidase mutants of Pseudomonas aeruginosa. Arch Microbiol 144: 228-322.
    • (1986) Arch Microbiol , vol.144 , pp. 228-322
    • Yang, T.1
  • 68
    • 0024379499 scopus 로고
    • The respiratory chains of pathogenic pseudomonads
    • Zannoni, D. (1989) The respiratory chains of pathogenic pseudomonads. Biochim Biophys Acta 975: 299-316.
    • (1989) Biochim Biophys Acta , vol.975 , pp. 299-316
    • Zannoni, D.1
  • 69
    • 0025873743 scopus 로고
    • Anaerobic growth and cyanide synthesis of Pseudomonas aeruginosa depend on anr, a regulatory gene homologous with fnr of Escherichia coli
    • Zimmerman, A., Reimann, C., Galimand, M., and Haas, D. (1991) Anaerobic growth and cyanide synthesis of Pseudomonas aeruginosa depend on anr, a regulatory gene homologous with fnr of Escherichia coli. Mol Microbiol 5: 1483-1490.
    • (1991) Mol Microbiol , vol.5 , pp. 1483-1490
    • Zimmerman, A.1    Reimann, C.2    Galimand, M.3    Haas, D.4


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